ProGT120 (PgfS)
| ProGT ID | ProGT120 (PgfS) |
| Organism Information | |
| Organism Name | Streptococcus mutans |
| Clinical Implication | Pathogenic |
| Domain | Bacteria |
| Classification | Phylum : Firmicutes Class : Bacilli Orders : Lactobacillales Family : Streptococcaceae Genus : Streptococcus Species : mutans |
| Taxonomic ID (NCBI) | 1309 |
| Genome Information | |
| Gene Information | |
| Gene Name | smu2067c (pgfS) |
| Protein information | |
| Protein Name | PgfS |
| Function in Native Organism | 1) PgfS is a glycosyltransferase required for glycosylation of collagen- and laminin-binding adhesin Cnm and wall-associated protein A (WapA). |
| Potential Application | 1) Pgf modification system could be a new target for the development of antibiotic against S. mutans and, possibly, other Streptococci. 2) Better understanding of how the Pgf system functions can potentially lead to the utilization of this system as a new tool in synthetic biology for the modification of recombinant proteins used for therapeutic and non-therapeutic purposes. |
| Additional Information | 1) PgfS is a GT-A type glycosyltransferase, it glycosylates the Cnm protein, which contributes to invasion of host cells and virulence in the G. mellonella model. 2) Posttranslational modification increases the proteolytic stability of Cnm and WapA. |
| Glycosyltransferase Information | |
| Glycosylation Type | O- (Ser/Thr) linked |
| EC Number (BRENDA) | 2.4.1.- |
| Mechanism of Glycan Transfer | Sequential |
| Donor Specificity | Nucleotide activated sugars |
| Accessory GT ID | ProGT120.1, ProGT120.2, ProGT120.3 |
| Glycan Information | |
| Experimental_strategies | In vivo |
| Acceptor Subtrate Information | |
| Acceptor Substrate name | WapA |
| ProGPdb ID | ProGP684 |
| Acceptor Substrate name | Cnm |
| ProGPdb ID | ProGP685 |
| Litrature | |
| Year Of Validation | 2018 |
| Reference | Avilés-Reyes, A., Freires, I.A., Besingi, R., Purushotham, S., Deivanayagam, C., Brady, L.J., Abranches, J. and Lemos, J.A., 2018. Characterization of the pgf operon involved in the posttranslational modification of Streptococcus mutans surface proteins. Scientific reports, 8(1), pp.1-12. |
| Corresponding Author | Department of Oral Biology, University of Florida, College of Dentistry, Gainesville, FL, USA. |
| Reference | Avilés-Reyes, A., Miller, J.H., Simpson-Haidaris, P.J., Hagen, F.K., Abranches, J. and Lemos, J.A., 2014. Modification of Streptococcus mutans Cnm by PgfS contributes to adhesion, endothelial cell invasion, and virulence. Journal of bacteriology, 196(15), pp.2789-2797. |
| Corresponding Author | 1 Center for Oral Biology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA. 2 Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA.
2 Center for Oral Biology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA.
3 Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA Department of Medicine/Hematology-Oncology Division, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA Department of Pathology and Laboratory Medicine, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA.
4 Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA.
5 Center for Oral Biology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA. |